A naturally occurring mini-alanyl-tRNA synthetase.

ABSTRACT: Alanyl-tRNA synthetase (AlaRS) retains a conserved prototype structure throughout its biology, consisting of catalytic, tRNA-recognition, editing, and C-Ala domains. The catalytic and tRNA-recognition domains catalyze aminoacylation, the editing domain hydrolyzes mischarged tRNA^Ala, and C-Ala-the major tRNA-binding module-targets the elbow of the L-shaped tRNA^Ala. Interestingly, a mini-AlaRS lacking the editing and C-Ala domains is recovered from the Tupanvirus of the amoeba Acanthamoeba castellanii. Here we show that Tupanvirus AlaRS (TuAlaRS) is phylogenetically related to its host's AlaRS. Despite lacking the conserved amino acid residues responsible for recognition of the identity element of tRNA^Ala (G3:U70), TuAlaRS still specifically recognized G3:U70

SUBMITTER: Antika TR 

PROVIDER: S-EPMC10036535 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature